BMRB Entry 30569

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30569
MolProbity Validation Chart

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Title:
Structure of the C-terminal Helical Repeat Domain of Eukaryotic Elongation Factor 2 Kinase (eEF-2K)
Deposition date:
2019-02-08
Original release date:
2019-05-24
Authors:
Piserchio, A.; Will, N.; Giles, D.; Hajredini, F.; Dalby, K.; Ghose, R.
Citation:

Citation: Piserchio, A.; Will, N.; Giles, D.; Hajredini, F.; Dalby, K.; Ghose, R.. "Solution Structure of the Carboxy-Terminal Tandem Repeat Domain of Eukaryotic Elongation Factor 2 Kinase and its Role in Substrate Recognition."  J. Mol. Biol. 431, 2700-2717 (2019).
PubMed: 31108082

Assembly members:

Assembly members:
entity_1, polymer, 167 residues, 18893.021 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET-26b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SHMGELEAIVGLGLMYSQLP HHILADVSLKETEENKTKGF DYLLKAAEAGDRQSMILVAR AFDSGQNLSPDRCQDWLEAL HWYNTALEMTDCDEGGEYDG MQDEPRYMMLAREAEMLFTG GYGLEKDPQRSGDLYTQAAE AAMEAMKGRLANQYYQKAEE AWAQMEE

Data typeCount
13C chemical shifts712
15N chemical shifts183
1H chemical shifts1124

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 167 residues - 18893.021 Da.

1   SERHISMETGLYGLULEUGLUALAILEVAL
2   GLYLEUGLYLEUMETTYRSERGLNLEUPRO
3   HISHISILELEUALAASPVALSERLEULYS
4   GLUTHRGLUGLUASNLYSTHRLYSGLYPHE
5   ASPTYRLEULEULYSALAALAGLUALAGLY
6   ASPARGGLNSERMETILELEUVALALAARG
7   ALAPHEASPSERGLYGLNASNLEUSERPRO
8   ASPARGCYSGLNASPTRPLEUGLUALALEU
9   HISTRPTYRASNTHRALALEUGLUMETTHR
10   ASPCYSASPGLUGLYGLYGLUTYRASPGLY
11   METGLNASPGLUPROARGTYRMETMETLEU
12   ALAARGGLUALAGLUMETLEUPHETHRGLY
13   GLYTYRGLYLEUGLULYSASPPROGLNARG
14   SERGLYASPLEUTYRTHRGLNALAALAGLU
15   ALAALAMETGLUALAMETLYSGLYARGLEU
16   ALAASNGLNTYRTYRGLNLYSALAGLUGLU
17   ALATRPALAGLNMETGLUGLU

Samples:

sample_1: eEF2K (562-725), [U-99% 13C; U-99% 15N], 200 ± 20 uM; sodium phosphate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 4 ± 0.4 mM; EDTA 0.2 ± 0.02 mM; AEBSF protease inhibitor 2 ± 0.02 mM

sample_2: eEF2K (562-725), [U-99% 13C; U-99% 15N], 400 ± 40 uM; sodium phosphate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 4 ± 0.4 mM; EDTA 0.2 ± 0.02 mM; AEBSF protease inhibitor 2 ± 0.02 mM

sample_3: eEF2K (562-725), [U-99% 13C; U-99% 15N], 340 ± 35 uM; sodium phosphate 14 ± 2 mM; sodium chloride 100 ± 5 mM; DTT 4 ± 0.4 mM; EDTA 0.2 ± 0.02 mM; AEBSF protease inhibitor 2 ± 0.2 mM; Pf1 phage 14 ± 2 mg/mL

sample_4: eEF2K (562-725), [U-99% 13C; U-99% 15N], 360 ± 36 uM; sodium phosphate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 4 ± 0.4 mM; EDTA 0.2 ± 0.02 mM; AEBSF protease inhibitor 2 ± 0.02 mM

sample_conditions_1: ionic strength: 120 mM; pH: 6.5; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
4D HC-HSQC-NOESY-HN-HSQCsample_4isotropicsample_conditions_1
3D 3D NNH (15N-HSQC-NOESY-15N-HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1
3D H-13C NOESY aromaticsample_4isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D Hcc(co)NHsample_2isotropicsample_conditions_1
3D hCc(co)NHsample_2anisotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 15N HSQC-IPAPsample_3anisotropicsample_conditions_1
3D IPAP-J-HNCOsample_3anisotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SMILE, Ying, J., Delaglio, F., Torchia, D. A. & Bax, A. - processing

NMRView, Johnson, One Moon Scientific - data analysis, peak picking

TALOSN, Shen, Y. & Bax, A. - data analysis

PALES, Zweckstetter, M - data analysis

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker AVANCE III 800 MHz
  • Bruker AVANCE III 700 MHz
  • Bruker AVANCE III 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks